The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s election without traverse of Group I, claims 1, 4-5, 8, 13, to enzyme sequence SEQ ID NO: 2, Bacillus, polyolefin, Bacillus subtilis, alkane, in the reply filed on June 11, 2026 is acknowledged.
Claims 7, 10-12, 14-15, 18-19 are canceled. Claims 2-3, 6, 9, 16-18, 20-27 have been withdrawn from further consideration by the examiner because they are drawn to non-elected inventions. Claims 1, 4-5, 8, 13, to enzyme sequence SEQ ID NO: 2, Bacillus, polyolefin, Bacillus subtilis, alkane, are under consideration.
Priority: This application is a 371 of PCT/FI2022/050090, filed February 15, 2022, which claims benefit to foreign application FI 20215157, filed February 16, 2021. A copy of the foreign priority document has been received in the instant application on August 14, 2023 and is in the English language.
Failure to Comply with Sequence Rules
Where the description of a patent application discusses a sequence of 4 or more amino acids or a sequence of 10 or more nucleic acids, reference must be made to the sequence by use of the sequence identifier preceded by “SEQ ID NO:” in the text of the description even if the sequence is also embedded in the text of the description of the patent application (see 37 CFR 1.821, especially paragraphs (a)-(d)). The sequence identifier may be used in either the drawing or the Brief Description of Drawings (see MPEP 2422).
Objection to the Drawings:
The drawings are objected to because at least Fig. 6 recites sequences without corresponding SEQ ID NOs. The sequences must be in computer readable form (CRF) for search. See MPEP 2422 for sequence compliance requirements. Appropriate correction is required.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code: see at least paragraphs 0141, 0145, 0187, 0193 (of the application publication US 20240228990). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 4-5, 8, 13 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
In analyzing the claims for compliance with the written description requirements of 35 U.S.C. 112, first paragraph, a determination is made as to whether the specification contains a written description sufficient to show they had possession of the full scope of their claimed invention at the time the application was filed. The factors to be considered include disclosure of a complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, and any combination thereof.
In the present situation, the claims are drawn to a method of degrading a hydrocarbon chain, the method comprising providing a material comprising a hydrocarbon chain and an enzyme or a fragment thereof capable of degrading the hydrocarbon chain, and allowing said enzyme or fragment thereof to degrade the hydrocarbon chain, wherein the enzyme or fragment thereof comprising amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2 wherein the enzyme is optionally genetically modified (claim 1 and dependent claims), where the enzyme has at least 20% percent sequence identity to SEQ ID NO: 2 (instant claim 5).
Accordingly, the claims encompass a significantly large genus of naturally occurring and mutant amino acid sequences having activity capable of degrading a hydrocarbon and sharing only a few amino acid residues with SEQ ID NO: 2 and/or having only at least 20% sequence identity with SEQ ID NO: 2.
However, the specification discloses specific enzymes, i.e. metal-dependent hydrolases, comprising specific amino acid sequences, having activity to degrade a hydrocarbon (see examples 1-5).
The specification does not disclose any particular variants, of SEQ ID NO: 2, having at least 20% sequence identity to SEQ ID NO: 2, and/or any particular variants comprising only of amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2, and which have activity capable of degrading a hydrocarbon. There is no guidance in the specification regarding which or what 80% may vary from SEQ ID NO: 2 and/or which other amino acid residues are present in the variants in addition to the amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2.
Therefore, the specification has described in terms of its complete structure only specific metal-dependent hydrolase polypeptides having activity to degrade a hydrocarbon.
The specification does not describe by other relevant identifying characteristics a representative number of additional species within the broadly claimed genus.
The state of the art is that predicting protein function is challenging and predictions based on sequence or structural homology can be inaccurate because even proteins with significant amino acid sequence identity can have different functions (Jeffrey p. 2-3). Proteins with small changes in amino acid sequence in or near the active site might not share the catalytic activity of other members of an enzyme family but instead might have a different function, such as a different catalytic mechanism or a different substrate (Jeffrey p. 3). With hundreds and even thousands of atoms that interact weakly with each other in an ensemble of closely related and interconverting folded conformations, the complex and finely tuned enzyme fades easily in the clumsy hands of the protein engineer (Arnold p. 253-254). A further problem is that amino acids care about their context - their neighbors influence their contributions to an enzyme's activity. Also, many important biocatalyst properties are not localized in a small number of catalytic residues, but reflect contributions from many residues distributed over large parts of the protein. Even when large functional changes can be obtained with a few amino acid substitutions, it will be often difficult or impossible to discern the specific mutations responsible (Arnold p. 254). Biocatalysts need to become predictable and routine tools. At present they are neither, and biocatalyst design is still more of an art than a science (Arnold p. 257).
It is noted that the specification also teaches the general methodology for performing mutagenesis to obtain enzyme variants and methods for measuring or detecting activity of degrading a hydrocarbon chain. However, possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features. See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895.
This finding is also emphasized in Ex Parte Kubin (No. 2007-0819, Bd. Pat. Ann. & Int. May 31. 2007), wherein it is stated that:
“Although there is often significant overlap” between the enablement and written description requirements, “they are nonetheless independent of each other.” University of Rochester, 358 F.3d at 921, 69 USPQ2d at 1891. An “invention may be enabled even though it has not been described.” Id. Such is the situation here. While we conclude one skilled in the art would have been able to make and use the full scope of claim 73 through routine experimentation, we find Appellants did not describe the invention of claim 73 sufficiently to show they had possession of the claimed genus of nucleic acids. See, e.g., Noelle v. Lederman, 355 F.3d 1343, 1348, 69 USPQ2d 1508, 1513 (Fed. Cir. 2004) (“invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed”).
Thereby, a showing of how to potentially identify and make other nucleic acids/polypeptides is not sufficient to establish that Applicants were in possession of the invention as broadly claimed.
The skilled artisan cannot necessarily envision the detailed structures of ALL variants comprising any amino acid sequence and sharing only some amino acids with SEQ ID NO: 2 and which have activity of degrading any hydrocarbon chain or the detailed structures of ALL derivatives of SEQ ID NO: 2, having at least 20% sequence identity, wherein the variant SEQ ID NO: 2 polypeptides have adequate activity of degrading any hydrocarbon chain because the specification provides minimal guidance as to which substitutions and/or deletions and/or additions and which amino acids are essential and critical for SEQ ID NO: 2 to have activity of degrading any hydrocarbon chain, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the methods of making the claimed invention. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating or making it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
Claims 1, 4-5, 8, 13 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method of degrading a specific hydrocarbon chain (polyolefin) comprising providing a material comprising the noted hydrocarbon and an enzyme comprising the amino acid sequence of SEQ ID NO: 2, and allowing the enzyme to degrade the noted hydrocarbon, does not reasonably provide enablement for a method of degrading any hydrocarbon chain comprising providing any material comprising any hydrocarbon chain and an enzyme or a fragment thereof capable of degrading the hydrocarbon chain, and allowing said enzyme or fragment thereof to degrade the hydrocarbon chain, wherein the enzyme or fragment thereof comprising amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2 wherein the enzyme is optionally genetically modified. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
The scope of the instant claims is not commensurate with the enablement of the instant disclosure, because practice of the claimed invention would require undue experimentation by an artisan of ordinary skill in the art to ascertain which enzyme variants comprising any amino acid sequence and sharing only some amino acids with SEQ ID NO: 2 will have sufficient activity to degrade any hydrocarbon chain, and/or which enzyme variants having 20% sequence identity to SEQ ID NO: 2 will have activity to degrade any hydrocarbon chain. The claims are drawn to a method of degrading a hydrocarbon chain, the method comprising providing a material comprising a hydrocarbon chain and an enzyme or a fragment thereof capable of degrading the hydrocarbon chain, and allowing said enzyme or fragment thereof to degrade the hydrocarbon chain, wherein the enzyme or fragment thereof comprising amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2 wherein the enzyme is optionally genetically modified (claim 1 and dependent claims), where the enzyme has at least 20% percent sequence identity to SEQ ID NO: 2 (instant claim 5). Accordingly, the claims encompass a significantly large genus of naturally occurring and mutant amino acid sequences having activity capable of degrading a hydrocarbon and sharing only a few amino acid residues with SEQ ID NO: 2 and/or having only at least 20% sequence identity with SEQ ID NO: 2. Thus, there could be a myriad variants where the variant SEQ ID NO: 2 polypeptides have sufficient activity to degrade any hydrocarbon. Therefore, for the instant claimed invention, it would require an undue burden of experimentation for a skilled artisan to determine exactly which derivatives or variants have activity to degrade which type of hydrocarbon when any type of material comprising a hydrocarbon is provided.
The factors to be considered in determining whether undue experimentation is required are summarized in In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). The court in Wands states: “'Enablement is not precluded by the necessity for some experimentation such as routine screening. However, experimentation needed to practice the invention must not be undue experimentation. The key word is 'undue,' not 'experimentation.' " (Wands, 8 USPQ2d 1404). Clearly, enablement of a claimed invention cannot be predicated on the basis of quantity of experimentation required to make or use the invention. ''Whether undue experimentation is needed is not a single, simple factual determination, but rather is a conclusion reached by weighing many factual considerations.” (Wands, 8 USPQ2d 1404). The factors to be considered in determining whether undue experimentation is required include: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims.
In the instant case the quantity of experimentation would be large since there are myriad substitutions and/or deletions and/or insertions and/or additions and amino acid residues to choose from to obtain variants of SEQ ID NO: 2, having sufficient activities to degrade which type of hydrocarbon when any type of material comprising a hydrocarbon is provided. The amount of guidance in the specification is minimal with regard to which amino acids in SEQ ID NO: 2 (a metal-dependent hydrolase) have activity with any type material comprising a hydrocarbon. In particular, the specification discloses specific enzymes, i.e. metal-dependent hydrolases, comprising specific amino acid sequences, having activity to degrade a hydrocarbon (see examples 1-5).
The specification does not disclose any particular variants, of SEQ ID NO: 2, having at least 20% sequence identity to SEQ ID NO: 2, and/or any particular variants comprising only of amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2, and which have activity capable of degrading a hydrocarbon. There is no guidance in the specification regarding which or what 80% may vary from SEQ ID NO: 2 and/or which other amino acid residues are present in the variants in addition to the amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2.
The nature of the invention is such that many different polypeptides that are substantially similar to SEQ ID NO: 2 may or may not have activity to degrade a hydrocarbon when any material comprising any hydrocarbon is provided. The state of the art is that predicting protein function is challenging and predictions based on sequence or structural homology can be inaccurate because even proteins with significant amino acid sequence identity can have different functions (Jeffrey p. 2-3). Proteins with small changes in amino acid sequence in or near the active site might not share the catalytic activity of other members of an enzyme family but instead might have a different function, such as a different catalytic mechanism or a different substrate (Jeffrey p. 3). With hundreds and even thousands of atoms that interact weakly with each other in an ensemble of closely related and interconverting folded conformations, the complex and finely tuned enzyme fades easily in the clumsy hands of the protein engineer (Arnold p. 253-254). A further problem is that amino acids care about their context - their neighbors influence their contributions to an enzyme's activity. Also, many important biocatalyst properties are not localized in a small number of catalytic residues, but reflect contributions from many residues distributed over large parts of the protein. Even when large functional changes can be obtained with a few amino acid substitutions, it will be often difficult or impossible to discern the specific mutations responsible (Arnold p. 254). Biocatalysts need to become predictable and routine tools. At present they are neither, and biocatalyst design is still more of an art than a science (Arnold p. 257).
The relative level of skill in this art is very high. The predictability as to what substantially similar protein will have which activity is zero.
In view of the overly broad scope of the claims, the lack of guidance and working examples provided in the specification, and the high degree of unpredictability as evidenced by the prior art, undue experimentation would be necessary for a skilled artisan to make and use the entire scope of the claimed invention. Applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of having the desired biological characteristics is unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 1, 4-5, 8, 13 are rejected under 35 U.S.C. 103 as being unpatentable over Jain et al. (2018 Bioremediation Journal 22(3-4): 73-90) in view of Berka et al. (WO 2008066931). Jain et al. disclose mostly commonly used plastics are polyolefins like polyethylene (PE) and propylene (PP), which are bioinert in nature due to their molecular weight, hydrophobicity, and lack of functional groups (at least p. 73). Jain et al. disclose that as the use of polymer is becoming unavoidable, there have to be ways to degrade these polymers (at least p. 73). Jain et al. disclose isolating PP degrading bacteria and that the PP degrading bacteria further selected for degradation abilities and identified for ability to degrade blends of PP and poly-L-lactide (PLLA) were identified as Bacillus species, where the isolated bacteria isolates P3 showed 99.8% similarity with B. cereus, isolate P6 showed 99.8% similarity with B. licheniformis, isolate P8 showed 99.6% similarity with B. thuringiensis, isolate P10 showed 99.6% similarity with B. thuringiensis, isolate P13 showed 99.7% similarity with B. cereus (at least p. 73, 79-82). Jain et al. disclose that the degradation ability was monitored by determining the growth of bacteria in minimal media supplemented with polymers at intervals of 24 hrs. (at least p. 80). Jain et al. disclose that the Bacillus species, including B. licheniformis, were able to grow and utilize the polymers as carbon source (at least p. 80-82). Jain et al. do not explicitly teach a B. licheniformis comprising an enzyme comprising the amino acid sequence of instant SEQ ID NO: 2.
Berka et al. disclose the complete genome of a B. licheniformis strain SJ1904 (ATCC PTA-7992) (at least p. 4-7). Berka et al. disclose that there are numerous industrial uses for B. licheniformis; the species has been used for decades in the manufacture of industrial enzymes, owing largely to its ability to secrete sizable amounts of degradative enzymes (at least p. 2). Berka et al. disclose that the chromosome of B. licheniformis serves as a reservoir of useful genes/proteins that have environmental, energy, health, and industrial applications (at least p. 74-75). Berka et al. disclose that the B. licheniformis strain SJ1904 comprises nucleic acid molecules encoding a polypeptide (SEQ ID NO: 8445), which has 100% sequence identity to instant SEQ ID NO: 2 (at least p. 26) (see also appendix A).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate the B. licheniformis strain SJ1904 for the B. licheniformis in the method for degrading blends of PP and PLLA of Jain et al., thereby arriving at the claimed method of degrading a hydrocarbon chain comprising providing a material comprising a hydrocarbon chain and an enzyme or a fragment thereof capable of degrading the hydrocarbon chain, and allowing said enzyme or fragment thereof to degrade the hydrocarbon chain, wherein the enzyme or fragment thereof comprising amino acids D23, H48, H50, D52, H53, H108, D143, corresponding to the amino acid positions presented in SEQ ID NO: 2 (instant claims 1, 4-5, 8, 13). The motivation to do so is given by the prior art, which disclose Bacillus species, including B. licheniformis, comprise enzymes able to degrade blends of polymers, including PP. One of ordinary skill would have a reasonable expectation of success because the prior art Jain et al. disclose Bacillus species, including B. licheniformis, are able to degrade PP blends and utilize the polymers as a carbon source and the prior art discloses other known B. licheniformis include the B. licheniformis strain SJ1904 of Berka et al.
Regarding instant claim 8, Jain et al. disclose B. licheniformis has the ability to degrade blends of PP and PLLA, where PP is polyolefin (at least p. 73, 80-82).
Regarding instant claim 13, Berka et al. disclose any of the polypeptides in the B. licheniformis strain SJ1904 can be modified (at least p. 36).
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Marsha Tsay whose telephone number is (571)272-2938. The examiner can normally be reached M-F.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao can be reached at 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Marsha Tsay/Primary Examiner, Art Unit 1656
Appendix A
ID AUR73316 standard; protein; 228 AA.
XX
AC AUR73316;
XX
DT 05-MAR-2009 (first entry)
XX
DE Bacillus licheniformis SJ1904 (ATCC PTA-7992) protein, SEQ ID 8445.
XX
KW Chromosome; BOND_PC; YtkL; metal-dependent hydrolase;
KW conserved protein YtkL.
XX
OS Bacillus licheniformis; SJ1904 (ATCC PTA-7992).
XX
CC PN WO2008066931-A2.
XX
CC PD 05-JUN-2008.
XX
CC PF 29-NOV-2007; 2007WO-US024746.
XX
PR 29-NOV-2006; 2006US-0861992P.
XX
CC PA (NOVO ) NOVOZYMES INC.
XX
CC PI Berka R, Rey M, Ramaiya P;
XX
DR WPI; 2008-H74169/49.
DR N-PSDB; AUR68441.
DR PC:NCBI; gi52004643.
XX
CC PT New Bacillus licheniformis encoding biologically active substance, useful
CC PT for environmental, energy, health and industrial applications.
XX
CC PS Claim 11; SEQ ID NO 8445; 322pp; English.
XX
CC The present invention relates to the complete chromosome sequence of
CC Bacillus licheniformis SJ1904 (ATCC PTA-7992). The present invention also
CC relates to isolated polynucleotides of the chromosome of Bacillus
CC licheniformis SJ1904 that encode biologically active substances (such as
CC the present sequence) and to nucleic acid constructs, vectors, and host
CC cells comprising the polynucleotides as well as methods for producing
CC biologically active substances encoded by the polynucleotides and to
CC methods of using the isolated polynucleotides of the complete chromosome
CC of Bacillus licheniformis SJ1904. The polynucleotides and polypeptides
CC are useful for environmental, energy, health and industrial applications.
CC The chromosome sequence of the invention is also useful for performing
CC comparative genomics and proteomics studies leading to improved
CC industrial strains as well as a better understanding of genome evolution
CC among closely-related bacilli in the subtilis-licheniformis group.
CC
CC Revised record issued on 26-FEB-2009 : Enhanced with precomputed
CC information from BOND.
XX
SQ Sequence 228 AA;
Query Match 100.0%; Score 1204; Length 228;
Best Local Similarity 100.0%;
Matches 228; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MKVAYHGHSVVTVDTGDHQLIFDPFITGNSLTDLKPEDVKADVILLTHGHNDHVGDTIEI 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MKVAYHGHSVVTVDTGDHQLIFDPFITGNSLTDLKPEDVKADVILLTHGHNDHVGDTIEI 60
Qy 61 AKRNNSLVVAPNELAVYLGWKGLNVHPMHIGGSHQFDFGKVKLTQAFHGSAYTEEDSQKI 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 AKRNNSLVVAPNELAVYLGWKGLNVHPMHIGGSHQFDFGKVKLTQAFHGSAYTEEDSQKI 120
Qy 121 VYTGMPAGILLTVEGRTIFHAGDTGLFSDMKLIGELNHIDLAFLPIGDNFTMGPEDAKLA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VYTGMPAGILLTVEGRTIFHAGDTGLFSDMKLIGELNHIDLAFLPIGDNFTMGPEDAKLA 180
Qy 181 AEWLRAKQVVPVHYSTFPVIEQDPHAFADSLPGGVGKVLEVGESIEFK 228
||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 AEWLRAKQVVPVHYSTFPVIEQDPHAFADSLPGGVGKVLEVGESIEFK 228
Prosecution Insights